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Hydrolysis of GTP to GDP by an mcm-associated and meab- and mmaa-like G-protein from mycobacterium tuberculosis

Analyse Hydrolysis of GTP to GDP by an mcm-associated and meab- and mmaa-like G-protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3P32
Type
protein
Length
306 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Probable GTPase RV1496/MT1543
EC
3.6.-.-
UniProt
P63577
Ligands
GDP
Pockets
4 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProbable GTPase RV1496/MT1543 (EC 3.6.-.-)protein30658% helix, 13% strandP63577

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · chains A
  • PGE · Triethylene glycol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11850.530.7824empty
21150.350.7317PGE
3680.320.7514empty
4500.300.7614empty

Compared structures

  • 3P32 · Hydrolysis of GTP to GDP by an MCM-associated and MeaB- and MMAA-like G-protein from… · the same entry in another collection · chain A against A, TM-score 1.00

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